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1. Full Text Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity
by Houde, Vanessa P and Ritorto, Maria Stella and Gourlay, Robert and Varghese, Joby and Davies, Paul and Shpiro, Natalia and Sakamoto, Kei and Alessi, Dario R
The Biochemical journal, ISSN 0264-6021, 02/2014, Volume 458, Issue 1, pp. 41 - 56
The LKB1 tumour suppressor protein kinase functions to activate two isoforms of AMPK (AMP-activated protein kinase) and 12 members of the AMPK-related family... 
Amino Acid Sequence | Phosphorylation | Humans | Protein-Serine-Threonine Kinases - genetics | Molecular Sequence Data | Protein Prenylation | Serine - metabolism | Animals | Adenylate Kinase - metabolism | HEK293 Cells | Cysteine - metabolism | Mice | Protein-Serine-Threonine Kinases - metabolism | STRAD, STE20-related kinase adaptor | ACC, acetyl-CoA carboxylase | PI3K, phosphoinositide 3-kinase | SIK3, salt-inducible kinase 3 | HEK, human embryonic kidney | AMPK, AMP-activated protein kinase | ARK5, AMPK-related protein kinase 5 | EDL, extensor digitorum longus | ERK, extracellular-signal-regulated kinase | HRP, horseradish peroxidase | PDK1, phosphoinositide-dependent kinase 1 | RSK, ribosomal S6 kinase | DMEM, Dulbecco's modified Eagle's medium | NUAK1, NUAK family, SNF1-like kinase | phenformin | BRSK, BR serine | SAD-A | threonine kinase | mTOR, mammalian target of rapamycin | Bub2 | HSP90, heat-shock protein 90 | GAPDH, glyceraldehyde-3-phosphate dehydrogenase | SAD-B kinase | MARK4, MAP | signal transduction | 5-amino-4-imidazolecarboxamide riboside (AICAR) | PKA, cAMP-dependent protein kinase | HA, haemagglutinin | BiP, immunoglobulin heavy-chain-binding protein | PH, pleckstrin homology | raptor, regulatory associated protein of mTOR | Cdc16) domain family, member 1 | TBC1D1, TBC (Tre-2 | BDNF, brain-derived neurotrophic factor | ACTH, adrenocorticotropic hormone | MAPKAPK, MAPKAP (MAPK-activated protein) kinase | MEF, mouse embryonic fibroblast | AICAR, 5-amino-4-imidazolecarboxamide riboside | AMP-activated protein kinase-related kinase (AMPK-related kinase) | monoclonal antibody | microtubule affinity-regulating kinase 4 | ER, endoplasmic reticulum | MAPK, mitogen-activated protein kinase
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2. Full Text Localization of AMP kinase is regulated by stress, cell density, and signaling through the MEK→ERK1/2 pathway
by Mohamed Kodiha and James G. Rassi and Claire M. Brown and Ursula Stochaj
American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 11/2007, Volume 293, Issue 5, pp. 1427 - 1436
5′-AMP-activated protein kinase (AMPK) serves as an energy sensor and is at the center of control for a large number of metabolic reactions, thereby playing a... 
5′-AMP-activated protein kinase | Nuclear transport | PHYSIOLOGY | ACTIVATED PROTEIN-KINASE | NUCLEAR-EXPORT | PHOSPHORYLATION | ACETYLATION | MECHANISMS | 5'-AMP-activated protein kinase | CELL BIOLOGY | IMPORT | nuclear transport | INHIBITION | DISEASE | GROWTH | Phosphorylation | Threonine - chemistry | Oxidative Stress | Serum - metabolism | Cell Count | Humans | Mitogen-Activated Protein Kinase 3 - antagonists & inhibitors | Cytoplasm - metabolism | Adenylate Kinase - chemistry | Cell Nucleus - enzymology | Cell Nucleus - metabolism | Time Factors | Adenylate Kinase - metabolism | Stress, Physiological - metabolism | Flavonoids - pharmacology | Active Transport, Cell Nucleus | MAP Kinase Kinase Kinases - antagonists & inhibitors | Cytoplasm - enzymology | Mitogen-Activated Protein Kinase 1 - antagonists & inhibitors | MAP Kinase Kinase Kinases - metabolism | Hot Temperature | Stress, Physiological - enzymology | Peptides - pharmacology | Karyopherins - metabolism | Mitogen-Activated Protein Kinase 3 - metabolism | Signal Transduction - drug effects | Protein Kinase Inhibitors - pharmacology | HeLa Cells | Mitogen-Activated Protein Kinase 1 - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism
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3. Full Text Expression of adenylate kinase fused MEK1R4F in Escherichia coli and its application in ERK phosphorylation
by Yang, Fang and Li, Hongtao
Biotechnology Letters, ISSN 0141-5492, 10/2017, Volume 39, Issue 10, pp. 1553 - 1558
To construct a highly expressed and active MEK1R4F (a constitutively active form of mitogen-activated protein kinase kinase 1) by fusion of soluble adenylate... 
Life Sciences | Biochemistry, general | Biotechnology | Phosphorylation | Purification | Microbiology | Adenylate kinase | Applied Microbiology | Mitogen-activated protein kinase kinase 1 (MEK1) | PATHWAYS | TRANSLOCATION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | SITES | MAP | Biocatalysis | Humans | MAP Kinase Kinase 1 - metabolism | Recombinant Fusion Proteins - metabolism | MAP Kinase Kinase 1 - genetics | Escherichia coli - genetics | Adenosine Triphosphate - metabolism | Adenylate Kinase - metabolism | Escherichia coli - metabolism | Protein Engineering | Adenosine Diphosphate - metabolism | Escherichia coli - growth & development | Adenylate Kinase - genetics | Mitogen-Activated Protein Kinases - metabolism | Escherichia coli | Physiological aspects | Genetic aspects | Observations | Gene expression | Protein kinases | Extracellular signal-regulated kinase | MAP kinase | Catalytic activity | Kinases | ADP | Proteins | E coli | Protein kinase | Protein folding | N-Terminus | Catalysis | Fusion protein | In vitro methods and tests
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4. Full Text Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor
by Nicholas S. Duesbery and Craig P. Webb and Stephen H. Leppla and Valery M. Gordon and Kurt R. Klimpel and Terry D. Copeland and Natalie G. Ahn and Marianne K. Oskarsson and Kenji Fukasawa and Ken D. Paull and George F. Vande Woude
Science, ISSN 0036-8075, 5/1998, Volume 280, Issue 5364, pp. 734 - 737
Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin,... 
Signal transduction | Antigens | Phosphorylation | Anthrax | Antibodies | Amino acids | Immunoblotting | Reports | Toxins | Oocytes | Cyclins | TRANSFORMATION | PROTEIN | TOXIN | INVITRO | MULTIDISCIPLINARY SCIENCES | COMPONENTS | BACILLUS-ANTHRACIS | INHIBITORS | ADENYLATE-CYCLASE | MAMMALIAN-CELLS | PROTECTIVE ANTIGEN | Sequence Deletion | Protein-Tyrosine Kinases - metabolism | Humans | Bacterial Toxins - toxicity | Metalloendopeptidases - metabolism | Bacillus anthracis - enzymology | MAP Kinase Kinase 2 | Recombinant Fusion Proteins - metabolism | MAP Kinase Kinase 1 | Protein-Tyrosine Kinases - genetics | Mitogen-Activated Protein Kinase Kinases | Enzyme Inhibitors - toxicity | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Protein-Tyrosine Kinases - chemistry | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Myelin Basic Protein - metabolism | Signal Transduction | Xenopus laevis | Protein-Serine-Threonine Kinases - genetics | Antigens, Bacterial | Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors | Metalloendopeptidases - toxicity | Bacterial Toxins - metabolism | Animals | Oocytes - physiology | Mice | Protein-Serine-Threonine Kinases - chemistry | Enzyme Activation | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Cell Line, Transformed | Protein-Tyrosine Kinases - antagonists & inhibitors | Research | Protein kinases | Bacteria, Pathogenic | Proteins | Bacteria | Disease | Cellular biology
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5. Full Text Opposite regulation of the mitochondrial apoptotic pathway by C2‐ceramide and PACAP through a MAP‐kinase‐dependent mechanism in cerebellar granule cells
by Falluel‐Morel, Anthony and Aubert, Nicolas and Vaudry, David and Basille, Magali and Fontaine, Marc and Fournier, Alain and Vaudry, Hubert and Gonzalez, Bruno J
Journal of Neurochemistry, ISSN 0022-3042, 12/2004, Volume 91, Issue 5, pp. 1231 - 1243
The sphingomyelin‐derived messenger ceramides provoke neuronal apoptosis through caspase‐3 activation, while the neuropeptide pituitary adenylate... 
Bax | Bcl‐2 | pituitary adenylate cyclase‐activating polypeptide | mitochondrial apoptotic pathway | JNK | ERK | Bcl-2 | Pituitary adenylate cyclase-activating polypeptide | Mitochondrial apoptotic pathway | NEURONAL APOPTOSIS | CYCLASE-ACTIVATING POLYPEPTIDE | SIGNALING PATHWAYS | pituitary adenylate cyclase-activating polypeptide | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEATH | CERAMIDE LEVELS | NEUROSCIENCES | CYTOCHROME-C | CASPASE-3 ACTIVATION | PITUITARY | ADENYLATE-CYCLASE | CEREBRAL-ISCHEMIA | Intracellular Signaling Peptides and Proteins - pharmacology | Benzimidazoles | Caspase 9 | Rats, Wistar | Cytosol - drug effects | JNK Mitogen-Activated Protein Kinases - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Carbocyanines | Dose-Response Relationship, Drug | Nerve Growth Factors - pharmacology | Mitogen-Activated Protein Kinase Kinases - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | RNA, Messenger - biosynthesis | Caspases - metabolism | Drug Interactions | MAP Kinase Kinase 4 | Time Factors | Neuropeptides - pharmacology | Neurotransmitter Agents - pharmacology | Reverse Transcriptase Polymerase Chain Reaction - methods | Caspase 3 | Neurons - drug effects | Pituitary Adenylate Cyclase-Activating Polypeptide | Animals, Newborn | Membrane Potentials - drug effects | Blotting, Western - methods | Cytochromes c - metabolism | Fluorescent Antibody Technique - methods | Cells, Cultured | Enzyme Inhibitors - pharmacology | Rats | Mitochondria - drug effects | bcl-2-Associated X Protein | Gene Expression Regulation - drug effects | Sphingosine - pharmacology | Sphingosine - analogs & derivatives | Animals | Signal Transduction - drug effects | Cerebellum - cytology | Mice | Models, Neurological | Mitochondria - physiology | Proto-Oncogene Proteins c-bcl-2 - genetics | Mitogen-Activated Protein Kinases - metabolism | Cerebellum | Enzyme Inhibitors | Cytochromes c | Neuropeptides | Cytosol | Life Sciences | Mitochondria | Toxicology | Mitogen-Activated Protein Kinase Kinases | Sphingosine | JNK Mitogen-Activated Protein Kinases | Mitogen-Activated Protein Kinases | Signal Transduction | Neurons | Gene Expression Regulation | Intracellular Signaling Peptides and Proteins | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Neurotransmitter Agents | Membrane Potentials | Nerve Growth Factors | Fluorescent Antibody Technique | Proto-Oncogene Proteins c-bcl-2 | Caspases | RNA, Messenger
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6. Full Text AMP kinase—mediated activation of the BH3-only protein Bim couples energy depletion to stress-induced apoptosis
by Caoimhín G. Concannon and Liam P. Tuffy and Petronela Weisová and Helena P. Bonner and David Dávila and Caroline Bonner and Marc C. Devocelle and Andreas Strasser and Manus W. Ward and Jochen H.M. Prehn
The Journal of Cell Biology, ISSN 0021-9525, 4/2010, Volume 189, Issue 1, pp. 83 - 94
Excitotoxicity after glutamate receptor overactivation induces disturbances in cellular ion gradients, resulting in necrosis or apoptosis. Excitotoxic necrosis... 
Proteins | Neuroscience | Messenger RNA | Neurons | Cell death | Cell nucleus | Small interfering RNA | Antibodies | Gene expression regulation | Apoptosis | GLUTAMATE NEUROTOXICITY | SIGNALING PATHWAYS | CORTICAL-NEURONS | N-TERMINAL KINASE | MITOCHONDRIAL DYSFUNCTION | PROMOTES NEURONAL SURVIVAL | CYTOCHROME-C RELEASE | TRANSCRIPTION FACTOR | METHYL-D-ASPARTATE | CELL-DEATH | CELL BIOLOGY | Proto-Oncogene Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Rats | Mice, Transgenic | Proto-Oncogene Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Microscopy, Confocal | Animals | Bcl-2-Like Protein 11 | Adenylate Kinase - metabolism | Cell Death | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Mice | Neurons - metabolism | Adenylate Kinase - genetics | Physiological aspects | Observations | Glutamate | Properties | Gene expression
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7. Full Text Hindbrain 5′-Adenosine Monophosphate-activated Protein Kinase Mediates Short-term Food Deprivation Inhibition of the Gonadotropin-releasing Hormone–Luteinizing Hormone Axis: Role of Nitric Oxide
by Shakya, Manita and Shrestha, Prem K and Briski, Karen P
Neuroscience, ISSN 0306-4522, 07/2018, Volume 383, pp. 46 - 59
Hindbrain-derived stimuli restrain the gonadotropin-releasing hormone (GnRH)–pituitary luteinizing hormone (LH) reproductive neuroendocrine axis during energy... 
norepinephrine | neuronal nitric oxide synthase | luteinizing hormone | GnRH-I | food deprivation | estradiol | GnRH-l | GLUCOPRIVIC INHIBITION | TRANSPORTER GENE-EXPRESSION | ARCUATE NUCLEUS | LACTATE INFUSION | NEUROSCIENCES | DORSAL VAGAL COMPLEX | NEUROPEPTIDE-Y | FEMALE RAT | MESSENGER-RNA | LOADING CONTROL | ESTROUS-CYCLE | Food Deprivation - physiology | Animals | Adenylate Kinase - metabolism | Gonadotropin-Releasing Hormone - metabolism | Neurosecretory Systems - metabolism | Rats | Rhombencephalon - metabolism | Female | Luteinizing Hormone - metabolism | Nitric Oxide - metabolism | Estradiol | Rats, Sprague-Dawley | Neuropeptide Y | Brain | Adenosine | RNA | Neurons | Glycoproteins | Glutamate | Neural networks | Nitric oxide | Luteinizing hormone | GABA | Intermedin | Adenylic acid | Protein kinases | KiSS1 | Food deprivation
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8. Full Text Protein kinase N2 regulates AMP kinase signaling and insulin responsiveness of glucose metabolism in skeletal muscle
by Ruby, Maxwell A and Riedl, Isabelle and Massart, Julie and Åhlin, Marcus and Zierath, Juleen R
American Journal of Physiology - Endocrinology and Metabolism, ISSN 0193-1849, 10/2017, Volume 313, Issue 4, pp. E483 - E491
Insulin resistance is central to the development of type 2 diabetes and related metabolic disorders. Because skeletal muscle is responsible for the majority of... 
Insulin resistance | Lipid metabolism | AMP kinase | Protein kinase N2 | Skeletal muscle | TARGET | ACTIVATION | PHYSIOLOGY | LIPID-METABOLISM | PHOSPHORYLATION | lipid metabolism | MECHANISMS | PRK2 | protein kinase N2 | INHIBITION | GTPASES | ENDOCRINOLOGY & METABOLISM | RHO | POTENTIAL EFFECTOR | skeletal muscle | insulin resistance | Protein Kinase C - genetics | Phosphorylation | Signal Transduction | Humans | Mice, Inbred C57BL | Male | Muscle, Skeletal - metabolism | Muscle Fibers, Skeletal - metabolism | Gene Knockdown Techniques | Triglycerides - metabolism | Animals | Glycogen - metabolism | Protein Kinase C - metabolism | Adenylate Kinase - metabolism | Quadriceps Muscle - cytology | Insulin Resistance - genetics | Glucose - metabolism | Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha - metabolism | Lipid Metabolism - genetics | Mice | Protein Biosynthesis - genetics | In Vitro Techniques | Fatty Acids - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Physiological aspects | Muscles | Glucose metabolism | Adenylic acid | Protein kinases | Type 2 diabetes | Glycogen | Triglycerides | Glucose | Fatty acids | Insulin | Dextrose | G proteins
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9. Full Text AMP Kinase Is Required for Mitochondrial Biogenesis in Skeletal Muscle in Response to Chronic Energy Deprivation
by Haihong Zong and Jian Ming Ren and Lawrence H. Young and Marc Pypaert and James Mu and Morris J. Birnbaum and Gerald I. Shulman
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2002, Volume 99, Issue 25, pp. 15983 - 15987
Mitochondrial biogenesis is a critical adaptation to chronic energy deprivation, yet the signaling mechanisms responsible for this response are poorly... 
Energy deprivation | Phosphates | Biological Sciences | Sodium | Transgenic animals | Grade point average | Muscles | Actins | Gene expression regulation | Creatine | Skeletal muscle | MP-activated protein kinase | Calcium/calmodulin-dependent protein kinase IV | β-guanidinopropionic acid | Peroxisome proliferator-activated γ receptor coactivator-1α | ACTIVATED PROTEIN-KINASE | NUCLEAR | MULTIDISCIPLINARY SCIENCES | GLUCOSE-TRANSPORT | ACETYL-COA CARBOXYLASE | AMP-activated protein kinase | AMINOLEVULINATE SYNTHASE EXPRESSION | CONTRACTILE ACTIVITY | calcium/calmodulin-dependent protein kinase IV | FATTY-ACID OXIDATION | ELECTRICAL-STIMULATION | peroxisome proliferator-activated gamma receptor coactivator-1 alpha | IN-VIVO | GENE-EXPRESSION | beta-guanidinopropionic acid | Propionates - pharmacology | Calcium-Calmodulin-Dependent Protein Kinase Type 4 | Guanidines - pharmacology | Muscle Proteins - deficiency | Genes, Dominant | Muscle, Skeletal - drug effects | Calcium-Calmodulin-Dependent Protein Kinases - biosynthesis | Enzyme Induction - drug effects | Mitochondria, Muscle - physiology | Adenylate Kinase - physiology | Calcium-Calmodulin-Dependent Protein Kinase Type 2 | Muscle Proteins - physiology | Muscle, Skeletal - enzymology | Calcium-Calmodulin-Dependent Protein Kinases - genetics | Muscle, Skeletal - ultrastructure | Mice, Transgenic | Transcription Factors - biosynthesis | Transcription Factors - genetics | Adenylate Kinase - deficiency | Gene Expression Regulation - drug effects | Muscle Proteins - genetics | Animals | Adenine Nucleotides - metabolism | Mice | Phosphocreatine - metabolism | Adenylate Kinase - genetics | Energy Metabolism - drug effects | Physiological aspects | Energy metabolism | Bioenergetics | calmodulin-dependent protein kinase IV | calcium | peroxisome proliferator-activated γ receptor coactivator-1α
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10. Full Text Resveratrol stimulates AMP kinase activity in neurons
by Biplab Dasgupta and Jeffrey Milbrandt
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 04/2007, Volume 104, Issue 17, pp. 7217 - 7222
Resveratrol is a polyphenol produced by plants that has multiple beneficial activities similar to those associated with caloric restriction (CR), such as... 
Neuronal protection | Neuronal energy | Caloric restriction | LIFE-SPAN | caloric restriction | neuronal energy | ACTIVATED PROTEIN-KINASE | MULTIDISCIPLINARY SCIENCES | DIETARY RESTRICTION | SACCHAROMYCES-CEREVISIAE | PROMOTES MITOCHONDRIAL BIOGENESIS | BETA | neuronal protection | GLUCOSE-METABOLISM | ENDOTHELIAL-CELLS | CELLULAR-ENERGY | CALORIE RESTRICTION | Neurons, Afferent - drug effects | Brain - enzymology | Male | Neurons - cytology | Mitochondria - drug effects | Stilbenes - pharmacology | Enzyme Activation - drug effects | Aminoimidazole Carboxamide - pharmacology | Neurons, Afferent - enzymology | Brain - drug effects | Ribonucleotides - pharmacology | Animals | Aminoimidazole Carboxamide - analogs & derivatives | Sirtuin 1 | Adenylate Kinase - metabolism | Neurons - enzymology | Mice | Phosphorylation - drug effects | Ganglia, Spinal - drug effects | Neurons - drug effects | Sirtuins - metabolism | Neurites - drug effects | Protein-Serine-Threonine Kinases - metabolism | Neuroplasticity | Research | Adenylic acid | Resveratrol | Biological Sciences
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11. Full Text Zipping and Unzipping of Adenylate Kinase: Atomistic Insights into the Ensemble of Open ↔ Closed Transitions
by Beckstein, Oliver and Denning, Elizabeth J and Perilla, Juan R and Woolf, Thomas B
Journal of Molecular Biology, ISSN 0022-2836, 2009, Volume 394, Issue 1, pp. 160 - 176
Adenylate kinase (AdK), a phosphotransferase enzyme, plays an important role in cellular energy homeostasis. It undergoes a large conformational change between... 
adenylate kinase | importance sampling | free energy | molecular dynamics | transitions | PROTEIN | TARGETED MOLECULAR-DYNAMICS | DOMAIN CLOSURE | MECHANISM | SCALE CONFORMATIONAL-CHANGES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CRYSTAL-STRUCTURES | NETWORK MODEL | STRING METHOD | FREE-ENERGY | Protein Structure, Tertiary | Salts - chemistry | Thermodynamics | Animals | Computer Simulation | Humans | Surface Properties | Fluorescence Resonance Energy Transfer | Crystallography, X-Ray | Adenylate Kinase - chemistry
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12. Full Text AMP kinase acts as a negative regulator of RANKL in the differentiation of osteoclasts
by Lee, Young-Sun and Kim, Yang-Soon and Lee, Sun-Young and Kim, Geun-Hyang and Kim, Beom-Jun and Lee, Seung-Hun and Lee, Ki-Up and Kim, Ghi-Su and Kim, Seung-Whan and Koh, Jung-Min
Bone, ISSN 8756-3282, 2010, Volume 47, Issue 5, pp. 926 - 937
Abstract Introduction AMP-activated protein kinase (AMPK) has been reported to stimulate differentiation and proliferation of osteoblasts, but the role of AMPK... 
Orthopedics | Bone resorption | RANKL | Osteoclast | AMP kinase | ACTIVATED PROTEIN-KINASE | BERBERINE | ALPHA | SKELETAL-MUSCLE | EPITHELIAL-CELLS | PATHWAY | ENDOTHELIAL-CELLS | IN-VIVO | ENDOCRINOLOGY & METABOLISM | RECEPTOR ACTIVATOR | KAPPA-B LIGAND | RNA, Small Interfering - genetics | Apoptosis - drug effects | Stilbenes - pharmacology | Osteoclasts - cytology | Cell Differentiation - genetics | RANK Ligand - pharmacology | Adenylate Kinase - metabolism | Resveratrol | Macrophage Colony-Stimulating Factor - pharmacology | Bone Resorption - chemically induced | Catechin - pharmacology | Osteogenesis - genetics | Pyrazoles - pharmacology | Cell Survival - drug effects | MAP Kinase Kinase Kinases - genetics | Metformin - pharmacology | Osteogenesis - drug effects | Cells, Cultured | MAP Kinase Kinase Kinases - metabolism | Pyrimidines - pharmacology | Reverse Transcriptase Polymerase Chain Reaction | Osteoclasts - metabolism | Blotting, Western | Mice, Inbred ICR | Animals | Cell Differentiation - drug effects | Adenylate Kinase - antagonists & inhibitors | Catechin - analogs & derivatives | Mice | Adenylate Kinase - genetics | Osteoclasts - drug effects | Phosphates | Macrophage colony stimulating factor | Transforming growth factors | Calcium-binding proteins | T cells | Protein kinases | Enzyme-linked immunosorbent assay | Protein binding | AKT protein
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